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Literature summary for 1.3.1.96 extracted from
- Structure-function mapping of key determinants for hydrocarbon biosynthesis by squalene and squalene synthase-like enzymes from the green alga Botryococcus braunii race B (2014), Biochemistry, 53, 7570-7581 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene SSL-2, sequence comparisons, recombinant expression of C-terminally truncated wild-type and mutant enzymes enzymes, lacking 87 amino acids, in Escherichia coli strain BL21(DE3) | Botryococcus braunii |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Y168A | site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type | Botryococcus braunii |
| Y168F | site-directed mutagenesis, mutant substrate specificity and activity compared to the wild-type | Botryococcus braunii |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | bound | Botryococcus braunii | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Botryococcus braunii |  |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Botryococcus braunii | squalene and botryococcene are branched-chain, triterpene compounds that arise from the head-tohead condensation of two molecules of farnesyl diphosphate to yield 1'-1 and 1'-3 linkages, respectively. Different enzymes are responsible for botryococcene and squalene biosynthesis in the green alga Botryococcus braunii race B. The specificity for the 1'-1 and 1'-3 linkages is controlled by residues in the active sites that can mediate catalytic specificity. Identification of several amino acid positions contributing to the rearrangement of the cyclopropyl intermediate to squalene, The same positions do not appear to be sufficient to account for the cyclopropyl rearrangement to give botryococcene, oerview | ? | - |
? | |
| presqualene diphosphate + NADPH + H+ | Botryococcus braunii | - |
squalene + diphosphate + NADP+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Botryococcus braunii | G0Y287 | race B | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | analysis of substrate specificity, overview | Botryococcus braunii | ? | - |
? | |
| additional information | squalene and botryococcene are branched-chain, triterpene compounds that arise from the head-tohead condensation of two molecules of farnesyl diphosphate to yield 1'-1 and 1'-3 linkages, respectively. Different enzymes are responsible for botryococcene and squalene biosynthesis in the green alga Botryococcus braunii race B. The specificity for the 1'-1 and 1'-3 linkages is controlled by residues in the active sites that can mediate catalytic specificity. Identification of several amino acid positions contributing to the rearrangement of the cyclopropyl intermediate to squalene, The same positions do not appear to be sufficient to account for the cyclopropyl rearrangement to give botryococcene, oerview | Botryococcus braunii | ? | - |
? | |
| presqualene diphosphate + NADPH + H+ | - |
Botryococcus braunii | squalene + diphosphate + NADP+ | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| SSL-2 | - |
Botryococcus braunii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Botryococcus braunii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.3 | - |
assay at | Botryococcus braunii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Botryococcus braunii | |
| NADPH | - |
Botryococcus braunii | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | proposed catalytic cascades for the enzyme-mediated biosynthesis of squalene and botryococcene, and molecular modeling of Botryococcus braunii botryococcene and squalene synthase enzymes, overview. Substrate docking and molecular modeling | Botryococcus braunii |
| physiological function | squalene and botryococcene are branched-chain, triterpene compounds that arise from the head-tohead condensation of two molecules of farnesyl diphosphate to yield 1'-1 and 1'-3 linkages, respectively | Botryococcus braunii |
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Release 2023.1 (January 2023)
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